R Recombinant
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Tyrosine Hydroxylase (A8Y7R) Rabbit mAb #13106
Filter:
- WB
- IF
Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with a construct expressing full-length human tyrosine hydroxylase (hTH; +), or extracts from PC-12 and KNRK cells, using Tyrosine Hydroxylase (A8Y7R) Rabbit mAb (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower).
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 55-60 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Related Products
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:50 - 1:250 |
| Immunofluorescence (Frozen) | 1:400 |
| Immunofluorescence (Immunocytochemistry) | 1:400 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Tyrosine Hydroxylase (A8Y7R) Rabbit mAb recognizes endogenous levels of total tyrosine hydroxylase protein.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human tyrosine hydroxylase protein.
Background
Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of the neurotransmitter dopamine and other catecholamines. TH functions as a tetramer, with each subunit composed of a regulatory and catalytic domain, and exists in several different isoforms (1,2). This enzyme is required for embryonic development since TH knockout mice die before or at birth (3). Levels of transcription, translation and post-translational modification regulate TH activity. The amino-terminal regulatory domain contains three serine residues: Ser9, Ser31, and Ser40. Phosphorylation at Ser40 by PKA positively regulates the catalytic activity of TH (4-6). Phosphorylation at Ser31 by CDK5 also increases the catalytic activity of TH through stabilization of TH protein levels (7-9).
- Kumer, S.C. and Vrana, K.E. (1996) J Neurochem 67, 443-62.
- Bodeau-Péan, S. et al. (1999) J Biol Chem 274, 3469-75.
- Kobayashi, K. et al. (1995) J Biol Chem 270, 27235-43.
- Lew, J.Y. et al. (1999) Mol Pharmacol 55, 202-9.
- Vié, A. et al. (1999) J Biol Chem 274, 16788-95.
- Lindgren, N. et al. (2000) J Neurochem 74, 2470-7.
- Moy, L.Y. and Tsai, L.H. (2004) J Biol Chem 279, 54487-93.
- Lehmann, I.T. et al. (2006) J Biol Chem 281, 17644-51.
- Saraf, A. et al. (2007) J Biol Chem 282, 573-80.
Pathways
Explore pathways related to this product.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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